Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-3-20
pubmed:abstractText
The oxidation of mercury vapor (Hg degrees) to divalent inorganic mercury (Hg2+) was studied in rat brain homogenates. By using a "degassing" method, it was possible to speciate the mercury present in the homogenate and, for the first time, to measure the rate of oxidation as a function of the substrate (Hg degrees) concentration. Mercury oxidation was first-order with respect to substrate concentration at all concentrations tested, and the first-order rate constant for the oxidation process was proportional to homogenate concentration. The role of catalase compound I in mercury vapor oxidation by brain homogenate was examined by observing the effects of two inhibitors of catalase (catalase compound I) on homogenate mercury-oxidizing activity and catalase activity. Sodium azide (50 mM) completely inhibited both mercury-oxidizing activity and catalase activity. Aminotriazole (3-amino-1H-1,2,4-triazole) (50 mM) completely inhibited only mercury-oxidizing activity; some residual catalase activity was found in the aminotriazole-treated homogenate. It was concluded that catalase compound I plays a major role in the oxidation of Hg degrees, but the possibility that catalase-independent pathways make a minor contribution cannot be excluded.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0887-2082
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
53-68
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
An examination of the oxidation of mercury vapor by rat brain homogenate.
pubmed:affiliation
Division of Toxicology, University of Rochester School of Medicine, NY.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.